Academic Journal
Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high-spin ferric peroxidase
| العنوان: | Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high-spin ferric peroxidase |
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| المؤلفون: | Soudi, Monika, Delporte, Cedric, Paumann Page, Martina, Pirker, Katharina F., Edenhofer, Eva, Stadlmayr, Gerhard, Furtmüller, Paul G., Van Antwerpen, Pierre, Obinger, Christian, Boudjeltia, Karim Zouaoui, BELLEI, Marzia, BATTISTUZZI, Gianantonio |
| المساهمون: | Soudi, Monika, Delporte, Cedric, Paumann Page, Martina, Pirker, Katharina F., Bellei, Marzia, Edenhofer, Eva, Stadlmayr, Gerhard, Battistuzzi, Gianantonio, Furtmüller, Paul G., Van Antwerpen, Pierre, Obinger, Christian, Boudjeltia, Karim Zouaoui |
| سنة النشر: | 2015 |
| المجموعة: | Archivio della ricerca dell'Università di Modena e Reggio Emilia (Unimore: IRIS) |
| مصطلحات موضوعية: | collagen, extracellular matrix protein, glycosylation, metalloenzyme, peroxidase, peroxidasin, vascular peroxidase |
| الوصف: | Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine crosslinks. The latter confer critical structural reinforcement to collagen IV scaffolds. Here hsPxd01 and various truncated variants lacking non-enzymatic domains were recombinantly expressed in HEK cell lines. The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure and unfolding pathway are reported. The homotrimeric ironprotein contains a covalently-bound ferric high-spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 mV at pH 7.0. Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM) of full-length hsPxd01 is rather low but increased upon truncation. This is discussed with respect to its structure and proposed biosynthetic function in collagen IV crosslinking. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | STAMPA |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/25713063; info:eu-repo/semantics/altIdentifier/wos/WOS:000353404500027; volume:290; issue:17; firstpage:10876; lastpage:10890; journal:JOURNAL OF BIOLOGICAL CHEMISTRY; http://hdl.handle.net/11380/1067330; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84928403603; http://www.jbc.org/content/290/17/10876 |
| DOI: | 10.1074/jbc.M114.632273 |
| الاتاحة: | http://hdl.handle.net/11380/1067330 https://doi.org/10.1074/jbc.M114.632273 http://www.jbc.org/content/290/17/10876 |
| Rights: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.AAC3C39B |
| قاعدة البيانات: | BASE |
| DOI: | 10.1074/jbc.M114.632273 |
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